Abstract

Membranes play a crucial role in almost all cellular phenomena, yet we know little about the molecular organization of these structures or the functions which they carry out. The lipid component of many natural membranes has been well characterized, but we know little about the protein component mainly because of the insoluble nature of these proteins which makes them difficult to purify and study. However, it is only the protein component of membranes which can confer the high degree of specificity necessary to carry out the complex functions associated with biological membranes. In addition, proteins must play an important role in membrane structure. Methods of affinity chromatography using CDP-diglyceride Sepharose have been developed in this laboratory to purify membrane bound enzymes of phospholipid metabolism. By using affinity chromatography the phosphatidylserine synthetase has been purified to homogeneity and the phosphatidylglycerophosphate synthetase to near homogeneity. The physical, chemical and enzymological properties of these purified enzymes will be characterized in order to better understand membrane function and membrane biogenesis as well as the control of cell growth.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM020478-13
Application #
3270032
Study Section
Biochemistry Study Section (BIO)
Project Start
1976-06-01
Project End
1987-06-30
Budget Start
1985-07-01
Budget End
1986-06-30
Support Year
13
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of Texas Health Science Center Houston
Department
Type
Schools of Medicine
DUNS #
City
Houston
State
TX
Country
United States
Zip Code
77225

  Publications

Dowhan, William (2017) Understanding phospholipid function: Why are there so many lipids? J Biol Chem 292:10755-10766
Rathmann, Claudia; Schlösser, Amelie S; Schiller, Jürgen et al. (2017) Tat transport in Escherichia coli requires zwitterionic phosphatidylethanolamine but no specific negatively charged phospholipid. FEBS Lett 591:2848-2858
Vitrac, Heidi; Dowhan, William; Bogdanov, Mikhail (2017) Effects of mixed proximal and distal topogenic signals on the topological sensitivity of a membrane protein to the lipid environment. Biochim Biophys Acta Biomembr 1859:1291-1300
Rowlett, Veronica W; Mallampalli, Venkata K P S; Karlstaedt, Anja et al. (2017) Impact of Membrane Phospholipid Alterations in Escherichia coli on Cellular Function and Bacterial Stress Adaptation. J Bacteriol 199:
Dowhan, William; Vitrac, Heidi; Bogdanov, Mikhail (2015) May the force be with you: unfolding lipid-protein interactions by single-molecule force spectroscopy. Structure 23:612-4
Zweytick, Dagmar; Japelj, Bostjan; Mileykovskaya, Eugenia et al. (2014) N-acylated peptides derived from human lactoferricin perturb organization of cardiolipin and phosphatidylethanolamine in cell membranes and induce defects in Escherichia coli cell division. PLoS One 9:e90228
Bogdanov, Mikhail; Dowhan, William; Vitrac, Heidi (2014) Lipids and topological rules governing membrane protein assembly. Biochim Biophys Acta 1843:1475-88
Dowhan, William (2013) A retrospective: use of Escherichia coli as a vehicle to study phospholipid synthesis and function. Biochim Biophys Acta 1831:471-94
Dowhan, William; Bogdanov, Mikhail (2012) Molecular genetic and biochemical approaches for defining lipid-dependent membrane protein folding. Biochim Biophys Acta 1818:1097-107
Dowhan, William; Bogdanov, Mikhail (2011) Lipid-protein interactions as determinants of membrane protein structure and function. Biochem Soc Trans 39:767-74

Showing the most recent 10 out of 15 publications